angiotensinogen
Rennin is very ineffective at 0 degrees. Its optimum temperature which it works in is body temperature (37oC). If the enzyme is heated up to 70 degrees then it will denature and have no effects at all.
its all to do with the milk proteins, caseins. the rennin makes them coagulate. you probbably never got any of that, im doing a planning task and its hard.
Casein is converted to caseinogen by active rennin in the presence of calcium ions. Rennin, also known as chymosin, acts on casein in milk to facilitate curd formation, which is essential in cheese production. The calcium ions help stabilize the casein micelles, allowing rennin to effectively cleave the casein protein. This process is key in dairy processing and the creation of various dairy products.
Rennin, also known as chymosin, is an enzyme found in the stomach lining of calves. It can be isolated from the stomachs of calves or produced using biotechnology. Rennin is used in cheese making to coagulate milk, separating it into curds and whey.
Yes, rennin is considered a biological catalyst because it acts to speed up the coagulation of milk proteins during the cheesemaking process. It primarily helps to convert milk protein (casein) into solid curds, aiding in the formation of cheese.
CI rennin?
Type your answer here.how to make rennin
rennin
Robert Tigerstedt in 1898
No. Rennin is derived fom rennet, which comes from a cows stomach.
Rennin is very ineffective at 0 degrees. Its optimum temperature which it works in is body temperature (37oC). If the enzyme is heated up to 70 degrees then it will denature and have no effects at all.
In the stomach
the optimal pH for rennin is around 1-2, as this closely resembles the acidic environment of the stomach where rennin is most commonly found. However rennin also works at neutral pH, although at a much lower level of reaction. This is necessary because sometimes the stomach is diluted by outside materials.
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